ID   MAOM_MOUSE              Reviewed;         589 AA.
AC   Q99KE1; Q3TBM8;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=NAD-dependent malic enzyme, mitochondrial;
DE            Short=NAD-ME;
DE            EC=1.1.1.38;
DE   AltName: Full=Malic enzyme 2;
DE   Flags: Precursor;
GN   Name=Me2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = pyruvate + CO(2) + NADH.
CC   -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese
CC       (By similarity).
CC   -!- ENZYME REGULATION: Subject to allosteric activation by fumarate
CC       (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- MISCELLANEOUS: This isoenzyme can also use NADP(+) but is more
CC       effective with NAD(+) (By similarity).
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
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DR   EMBL; AK042289; BAC31216.1; -; mRNA.
DR   EMBL; AK050933; BAC34467.1; -; mRNA.
DR   EMBL; AK050980; BAC34483.1; -; mRNA.
DR   EMBL; AK156403; BAE33701.1; -; mRNA.
DR   EMBL; AK171157; BAE42281.1; -; mRNA.
DR   EMBL; BC004709; AAH04709.1; -; mRNA.
DR   IPI; IPI00115977; -.
DR   RefSeq; NP_663469.1; -.
DR   UniGene; Mm.36817; -.
DR   HSSP; P23368; 1GZ3.
DR   SMR; Q99KE1; 21-573.
DR   PhosphoSite; Q99KE1; -.
DR   REPRODUCTION-2DPAGE; Q99KE1; -.
DR   PRIDE; Q99KE1; -.
DR   Ensembl; ENSMUSG00000024556; Mus musculus.
DR   GeneID; 107029; -.
DR   KEGG; mmu:107029; -.
DR   MGI; MGI:2147351; Me2.
DR   HOGENOM; Q99KE1; -.
DR   HOVERGEN; Q99KE1; -.
DR   OMA; Q99KE1; QALRFHR.
DR   BRENDA; 1.1.1.38; 244.
DR   NextBio; 358536; -.
DR   ArrayExpress; Q99KE1; -.
DR   Bgee; Q99KE1; -.
DR   CleanEx; MM_ME2; -.
DR   GermOnline; ENSMUSG00000024556; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016619; F:malate dehydrogenase (oxaloacetate-decarbox...; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N.
DR   InterPro; IPR012302; Malic_NAD_bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Metal-binding; Mitochondrion; NAD; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1     18       Mitochondrion (By similarity).
FT   CHAIN        19    589       NAD-dependent malic enzyme,
FT                                mitochondrial.
FT                                /FTId=PRO_0000018538.
FT   NP_BIND     311    328       NAD (By similarity).
FT   ACT_SITE    112    112       Proton donor (By similarity).
FT   ACT_SITE    183    183       Proton acceptor (By similarity).
FT   METAL       255    255       Divalent metal cation (By similarity).
FT   METAL       256    256       Divalent metal cation (By similarity).
FT   METAL       279    279       Divalent metal cation (By similarity).
FT   BINDING     165    165       NAD (By similarity).
FT   BINDING     279    279       NAD (By similarity).
FT   BINDING     421    421       NAD (By similarity).
FT   SITE        279    279       Important for activity (By similarity).
SQ   SEQUENCE   589 AA;  65799 MW;  CD77AD5744B08CAB CRC64;
     MFSRLRAVTT PCTLTCRRVH LKEKGKPLML NPRTNKGMAF TLQERQMLGL QGLLPPKIET
     QDIQALRFHR NLKKMTSPLE KYIYIMGIQE RNEKLFYRIL QDDIESLMPI VYTPTVGLAC
     CQYGHIFRRP KGLFISISDR GHVRSIVDNW PENHVKAVVV TDGERILGLG DLGVYGMGIP
     VGKLCLYTAC AGIQPEKCLP VCIDVGTDNM ALLKDPFYMG LYQKRDRSQL YDDLMDEFMK
     AITDRYGRNT LIQFEDFGNH NAFRFLRKYQ QKYCTFNDDI QGTAAVALSG LLAAQRVINK
     PVSEHKILFL GAGEAALGIA NLIVLSMVES GLSEEEAQRK IWMFDKSGLL VKGRTASIDS
     NQEPYAHAAP ESIPATFEDA VNKLKPSVII GVAGAGPLFT HGVIKAMASI NERPIIFALS
     NPTAQAECTA EDAYTLTEGR CLFASGSPFE PVKLQDGRVF TPGQGNNAYI FPGVALAVIL
     CEARHISDTV FLEAAKALTT QLTDAELAQG RLYPSLANIQ EVSANIAIKL AEYLYANKMA
     FRYPEPEDKA RYVRERIWRS NYVSLLPDVY DWPESSLTPP QITEEKLPH
//